β1,6-N-acetylglucosamine-branched N-glycan

β1,6-N-acetylglucosamine-branched N-glycans are complex carbohydrate branches attached via β1,6 linkage to the mannose core of N-glycans on glycoproteins, catalyzed by the enzyme N-acetylglucosaminyltransferase-V (GnT-V or MGAT5)[3][6]. Their presence increases the structural complexity of cell-surface and secreted proteins and is associated with enhanced cell migration, signaling, and tumor metastasis. In cancer, increased β1,6-branched N-glycans correlate with tumor malignancy, promote metastasis via modification of receptors (e.g., integrins, growth factor receptors), and facilitate immune evasion through glycosylation of immune checkpoint proteins such as PD-L1[4][7]. These structures are considered key biomarkers and potential therapeutic targets due to their prominent role in disease progression[3][4][6].

Other names

Beta-1,6-GlcNAc-branched N-glycanMGAT5 productGnT-V productβ1,6-branch N-glycan

Inhibition of MGAT5/GnT-V reduces β1,6-branching, affecting cell signaling, adhesion, and tumor cell immune evasion. Modulation of glycan branching on immune checkpoint molecules (e.g., PD-L1), impacting binding to receptors like PD-1